title: Activity-based probes as a tool for functional proteomic analysis of proteases.
abstract: Traditional proteomics methodology allows global analysis of protein abundance but does not provide information on the regulation of protein activity. Proteases, in particular, are known for their multilayered post-translational activity regulation that can lead to a significant difference between protease abundance levels and their enzyme activity. To address these issues, the field of activity-based proteomics has been established in order to characterize protein activity and monitor the functional regulation of enzymes in complex proteomes. In this review, we present structural features of activity-based probes for proteases and discuss their applications in proteomic profiling of various catalytic classes of proteases.
authors.affiliation: Department of Biochemistry, Molecular and Structural Biology, JoZef Stefan Institute, Jamova Cesta 39, SI-1000 Ljubljana, Slovenia. marko.fonovic@ijs.si
authors.forename: Marko
authors.initials: M
authors.lastname: Fonović
authors.forename: Matthew
authors.initials: M
authors.lastname: Bogyo
mesh_terms: D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D045726:Metalloproteases / Q000737:chemistry / Q000378:metabolism; D015335:Molecular Probes / Q000737:chemistry*; D015394:Molecular Structure; D010447:Peptide Hydrolases / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism
chemical_list: D015335:Molecular Probes; D045726:Metalloproteases; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; D003546:Cysteine Endopeptidases